Pub Date : 2022-06-01DOI: 10.1080/10242422.2022.2082871
O. Almaghrabi, Y. Almulaiky
Abstract Alginate is a biomaterial that is considered suitable for enzyme immobilization. The biocompatibility and characteristics of the immobilized system can be improved by combining alginate with magnetite Fe3O4 nanoparticles. Therefore, the current study investigated the effect of magnetite Fe3O4 NPs on urease immobilization using different concentrations of magnetite Fe3O4 NPs. The morphological features for alginate/magnetite Fe3O4 NPs before and after immobilization were studied using an SEM, TGA, and FTIR. The reusability, half-life, enzymatic kinetics, and storage stability of the enzyme were all enhanced. The immobilization efficiency was determined to be 91% at optimal conditions. The immobilized urease was reused 20 times and a recovery of 59% of the initial activity. The soluble and immobilized urease was stored at 4 °C for 12 weeks and preserved 13% and 49% of the initial activities, respectively. The optimum pH for soluble and immobilized urease activity was estimated to be 7. The optimum temperature for soluble and immobilized urease activity was found to be 35 °C and 40 °C, respectively. The kinetics parameters showed the Vmax of 4.4 and 3.1 μmol/ml·min and the Km of 49.5 and 54.6 mM for the soluble and immobilized urease, respectively. Immobilized urease had a half-life of 11–20 min. The activation energy (Ea) of immobilized urease was determined to be 32 kJ K−1 mol−1, indicating that a small quantity of energy is required to produce the activated complex of substrate hydrolysis.
{"title":"A biocatalytic system obtained via immobilization of urease onto magnetic metal/alginate nanocomposite: Improving reusability and enhancing stability","authors":"O. Almaghrabi, Y. Almulaiky","doi":"10.1080/10242422.2022.2082871","DOIUrl":"https://doi.org/10.1080/10242422.2022.2082871","url":null,"abstract":"Abstract Alginate is a biomaterial that is considered suitable for enzyme immobilization. The biocompatibility and characteristics of the immobilized system can be improved by combining alginate with magnetite Fe3O4 nanoparticles. Therefore, the current study investigated the effect of magnetite Fe3O4 NPs on urease immobilization using different concentrations of magnetite Fe3O4 NPs. The morphological features for alginate/magnetite Fe3O4 NPs before and after immobilization were studied using an SEM, TGA, and FTIR. The reusability, half-life, enzymatic kinetics, and storage stability of the enzyme were all enhanced. The immobilization efficiency was determined to be 91% at optimal conditions. The immobilized urease was reused 20 times and a recovery of 59% of the initial activity. The soluble and immobilized urease was stored at 4 °C for 12 weeks and preserved 13% and 49% of the initial activities, respectively. The optimum pH for soluble and immobilized urease activity was estimated to be 7. The optimum temperature for soluble and immobilized urease activity was found to be 35 °C and 40 °C, respectively. The kinetics parameters showed the Vmax of 4.4 and 3.1 μmol/ml·min and the Km of 49.5 and 54.6 mM for the soluble and immobilized urease, respectively. Immobilized urease had a half-life of 11–20 min. The activation energy (Ea) of immobilized urease was determined to be 32 kJ K−1 mol−1, indicating that a small quantity of energy is required to produce the activated complex of substrate hydrolysis.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"456 - 465"},"PeriodicalIF":1.8,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47825227","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-05-24DOI: 10.1080/10242422.2022.2078661
Chiedu E. Edoamodu, Uchechukwu U. Nwodo
Purified crude laccase of Enterobacter sp. Kamsi and Bacillus sp. NU2 in the hybrid and combined form was immobilized on sodium alginate beads and applied to decolourize various textile dyes throug...
{"title":"Thermo-active and alkaliphilic amalgamated laccase immobilized on sodium alginate for synthetic dye decolourization","authors":"Chiedu E. Edoamodu, Uchechukwu U. Nwodo","doi":"10.1080/10242422.2022.2078661","DOIUrl":"https://doi.org/10.1080/10242422.2022.2078661","url":null,"abstract":"Purified crude laccase of Enterobacter sp. Kamsi and Bacillus sp. NU2 in the hybrid and combined form was immobilized on sodium alginate beads and applied to decolourize various textile dyes throug...","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"44 1","pages":""},"PeriodicalIF":1.8,"publicationDate":"2022-05-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138515800","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-05-18DOI: 10.1080/10242422.2022.2073226
L. Aguiar, E. Silva, J. David
Abstract Chalcones and flavanones are both present as secondary metabolites in edible and medicinal plants as isomers. Mostly of them are isolated in low yields from natural sources, along with the difficulties faced by the total synthesis, make them attractive for biotechnological studies in order to obtain new derivatives. Prompted by the enormous pharmacological interest in chalcones and flavanones compounds, their alimentary and chemical applications, this review covers their biotransformation as an alternative way for achieving chemical analogues with high selectivity, using mild and eco-friendly conditions. Stereoselective bioreductions of chalcones were the most reported biotransformation reactions, and they could be performed by bacteria, cyanobacteria, non-conventional yeasts (NCYs), and fungi strains with good yields. Flavanones have also been derivatized under stereochemical control by several microorganisms. All reported biotransformations contribute to increasing the availability of new and valuable leads for the market and industrial fields.
{"title":"Biotransformation of chalcones and flavanones: An update on their bio-based derivatizations","authors":"L. Aguiar, E. Silva, J. David","doi":"10.1080/10242422.2022.2073226","DOIUrl":"https://doi.org/10.1080/10242422.2022.2073226","url":null,"abstract":"Abstract Chalcones and flavanones are both present as secondary metabolites in edible and medicinal plants as isomers. Mostly of them are isolated in low yields from natural sources, along with the difficulties faced by the total synthesis, make them attractive for biotechnological studies in order to obtain new derivatives. Prompted by the enormous pharmacological interest in chalcones and flavanones compounds, their alimentary and chemical applications, this review covers their biotransformation as an alternative way for achieving chemical analogues with high selectivity, using mild and eco-friendly conditions. Stereoselective bioreductions of chalcones were the most reported biotransformation reactions, and they could be performed by bacteria, cyanobacteria, non-conventional yeasts (NCYs), and fungi strains with good yields. Flavanones have also been derivatized under stereochemical control by several microorganisms. All reported biotransformations contribute to increasing the availability of new and valuable leads for the market and industrial fields.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"40 1","pages":"393 - 412"},"PeriodicalIF":1.8,"publicationDate":"2022-05-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43957047","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-05-11DOI: 10.1080/10242422.2022.2073227
N. Aminudin, Nurul Aqilah Amran, Zaima Azira Zainal Abidin, D. Susanti
Abstract Curcumin has been widely acclaimed for several pharmacological properties, such as antioxidant, antimicrobial, anticancer, and anti-inflammation. Curcumin’s poor aqueous solubility, bioavailability, and cellular uptake hamper its ability to display maximum pharmacological effect in the human body. Synthesis of curcumin analogues to enhance its properties can be achieved through biotransformation. Greener, simpler, and higher selectivity and specificity make biotransformation an alternative approach when preparing curcumin analogues for the structure–activity relationship (SAR) study intended for drug design. This work systematically reviews the biotransformation of curcumin by utilizing fungi, gut microbiota, and enzymes. The SAR study of curcumin and its analogues for several bioactivities is also highlighted. Graphical Abstract
{"title":"Biotransformation of curcumin and structure–activity relationship (SAR) of its analogues: A systematic review","authors":"N. Aminudin, Nurul Aqilah Amran, Zaima Azira Zainal Abidin, D. Susanti","doi":"10.1080/10242422.2022.2073227","DOIUrl":"https://doi.org/10.1080/10242422.2022.2073227","url":null,"abstract":"Abstract Curcumin has been widely acclaimed for several pharmacological properties, such as antioxidant, antimicrobial, anticancer, and anti-inflammation. Curcumin’s poor aqueous solubility, bioavailability, and cellular uptake hamper its ability to display maximum pharmacological effect in the human body. Synthesis of curcumin analogues to enhance its properties can be achieved through biotransformation. Greener, simpler, and higher selectivity and specificity make biotransformation an alternative approach when preparing curcumin analogues for the structure–activity relationship (SAR) study intended for drug design. This work systematically reviews the biotransformation of curcumin by utilizing fungi, gut microbiota, and enzymes. The SAR study of curcumin and its analogues for several bioactivities is also highlighted. Graphical Abstract","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"1 - 14"},"PeriodicalIF":1.8,"publicationDate":"2022-05-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49003739","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-05-11DOI: 10.1080/10242422.2022.2070430
A. Solís, Abraham Cano, R. M. Martínez-Cásares, M. Solís-Oba, R. Castro-Rivera, Oscar Velázquez Flores
Abstract The HNL from the defatted meal of the seeds of Pouteria sapota (PsHNL) was extracted with water, and the aqueous extract was immobilized over celite or lyophilized and used as semi-purified PsHNL. The aqueous extract was mixed with celite, ratios 1:1, 1:2 and 1:4, and lyophilized. The immobilized PsHNLdir-celite catalysed the addition of HCN to 1b in buffer saturated-DIPE (microaqueous system) with high enantioselectivity in the first cycle but diminished in the next two cycles, best results were obtained with the ratio 1:4. The reaction with PsHNLdir-celite in biphasic medium (5% citrates buffer) improved the conversion compared with the microaqueous system, but it was still lower to that obtained with the PsHNL. Other way of immobilization studied was the precipitation of the enzyme with acetone and immobilization on celite, the PsHNLpp-celite catalysed the enantioselective addition of HCN to 2-fluoro (1a), 2-chloro (1b), 2-bromo (1c), 2-methyl (1d) and 2-nitro (1e) benzaldehydes, in the biphasic medium (1:4 ratio, 5% citrates buffer). The enantiomeric excess (ee) of (R)-2a, (R)-2b, (R)-2c and (R)-2d were >98% and remained during the three cycles. The ee of 2-nitromandelonitrile was 82% and was raised to 95% in the third cycle. Compared with the PsHNL, the conversion of 1a and 1b diminished 6% and 40%, respectively, after third cycle; for 2c, conversion was almost 10% higher in the first two cycles and diminished 19% in the third; for 2d and 2e the conversion was between 18–13% and 31–18% higher, respectively.
{"title":"Preparation of optically active cyanohydrins from 2-substituted benzaldehydes using a hydroxynitrile lyase from Pouteria sapota seeds immobilized on celite","authors":"A. Solís, Abraham Cano, R. M. Martínez-Cásares, M. Solís-Oba, R. Castro-Rivera, Oscar Velázquez Flores","doi":"10.1080/10242422.2022.2070430","DOIUrl":"https://doi.org/10.1080/10242422.2022.2070430","url":null,"abstract":"Abstract The HNL from the defatted meal of the seeds of Pouteria sapota (PsHNL) was extracted with water, and the aqueous extract was immobilized over celite or lyophilized and used as semi-purified PsHNL. The aqueous extract was mixed with celite, ratios 1:1, 1:2 and 1:4, and lyophilized. The immobilized PsHNLdir-celite catalysed the addition of HCN to 1b in buffer saturated-DIPE (microaqueous system) with high enantioselectivity in the first cycle but diminished in the next two cycles, best results were obtained with the ratio 1:4. The reaction with PsHNLdir-celite in biphasic medium (5% citrates buffer) improved the conversion compared with the microaqueous system, but it was still lower to that obtained with the PsHNL. Other way of immobilization studied was the precipitation of the enzyme with acetone and immobilization on celite, the PsHNLpp-celite catalysed the enantioselective addition of HCN to 2-fluoro (1a), 2-chloro (1b), 2-bromo (1c), 2-methyl (1d) and 2-nitro (1e) benzaldehydes, in the biphasic medium (1:4 ratio, 5% citrates buffer). The enantiomeric excess (ee) of (R)-2a, (R)-2b, (R)-2c and (R)-2d were >98% and remained during the three cycles. The ee of 2-nitromandelonitrile was 82% and was raised to 95% in the third cycle. Compared with the PsHNL, the conversion of 1a and 1b diminished 6% and 40%, respectively, after third cycle; for 2c, conversion was almost 10% higher in the first two cycles and diminished 19% in the third; for 2d and 2e the conversion was between 18–13% and 31–18% higher, respectively.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"344 - 352"},"PeriodicalIF":1.8,"publicationDate":"2022-05-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48062976","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-05-02DOI: 10.1080/10242422.2022.2068371
A. M. Baron, Ricardo de Sousa Rodrigues, Luis Guilherme Giannina Sante, Jocácia Muriele de Miranda Kister, Valéria Marta Gomes do Nascimento, Alesandro Bail
Abstract Metal-organic frameworks (MOFs) are versatile materials because they have a large internal surface area and tuneable pores, making them suitable for enzyme immobilization. In this study, we prepared a typical microporous Fe-BDC MOF through a thermal treatment to produce additional meso and macropores interconnected to each other, capable of immobilizing the Burkholderia lata LBBIO-BL02 (BLL) lipase by entrapment and physical adsorption. The immobilization efficiency (E) was 90%, and the activity retention (R) was 400% (pNPP hydrolysis). The immobilized lipase (BLL@BDC) also showed excellent activity in the hydrolysis of vegetable oils in aqueous medium, achieving up to 3,200 U g−1 for olive oil, as well as high stability in organic solvents, especially for polar ones, such as iso-propanol (101.5 ± 2.6%), ethanol (103.0 ± 6.0%) and acetone (107.7 ± 8.3%). The results indicate that the multiporous Fe-BDC MOF is a promising support for lipase immobilization and further application in biocatalysis performed in organic media. Graphical Abstract
摘要金属有机框架（MOFs）是一种多用途材料，因为它们具有大的内表面积和可调谐的孔，使其适合于酶固定化。在本研究中，我们通过热处理制备了一种典型的微孔Fe-BDC-MOF，以产生额外的相互连接的中孔和大孔，能够通过包埋和物理吸附固定拉塔伯克霍尔德菌LBBIO-BL02（BLL）脂肪酶。固定化效率（E）为90%，活性保留率（R）为400%（pNPP水解）。固定化脂肪酶(BLL@BDC)在水性介质中对植物油的水解也表现出优异的活性，达到3200 U g−1用于橄榄油，以及在有机溶剂中的高稳定性，特别是对于极性溶剂，如异丙醇（101.5 ± 2.6%）、乙醇（103.0 ± 6.0%）和丙酮（107.7 ± 8.3%）。结果表明，多孔Fe-BDC-MOF是一种很有前途的脂肪酶固定化载体，并在有机介质中的生物催化中进一步应用。图形摘要
{"title":"Metal-organic framework based on iron and terephthalic acid as a multiporous support for lipase Burkholderia lata LBBIO-BL02 and its potential for biocatalysis","authors":"A. M. Baron, Ricardo de Sousa Rodrigues, Luis Guilherme Giannina Sante, Jocácia Muriele de Miranda Kister, Valéria Marta Gomes do Nascimento, Alesandro Bail","doi":"10.1080/10242422.2022.2068371","DOIUrl":"https://doi.org/10.1080/10242422.2022.2068371","url":null,"abstract":"Abstract Metal-organic frameworks (MOFs) are versatile materials because they have a large internal surface area and tuneable pores, making them suitable for enzyme immobilization. In this study, we prepared a typical microporous Fe-BDC MOF through a thermal treatment to produce additional meso and macropores interconnected to each other, capable of immobilizing the Burkholderia lata LBBIO-BL02 (BLL) lipase by entrapment and physical adsorption. The immobilization efficiency (E) was 90%, and the activity retention (R) was 400% (pNPP hydrolysis). The immobilized lipase (BLL@BDC) also showed excellent activity in the hydrolysis of vegetable oils in aqueous medium, achieving up to 3,200 U g−1 for olive oil, as well as high stability in organic solvents, especially for polar ones, such as iso-propanol (101.5 ± 2.6%), ethanol (103.0 ± 6.0%) and acetone (107.7 ± 8.3%). The results indicate that the multiporous Fe-BDC MOF is a promising support for lipase immobilization and further application in biocatalysis performed in organic media. Graphical Abstract","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"332 - 343"},"PeriodicalIF":1.8,"publicationDate":"2022-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48516749","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-03-31DOI: 10.1080/10242422.2022.2056450
Arastoo Badoei-dalfard, Mahla Saeed, Z. Karami
Abstract In this paper, a Serratia marcescens fibrinolytic protease KD was covalently immobilized onto the electrospun prepared glutaraldehyde (GA)-functionalized chitosan/cellulose acetate membrane nanofibres. Enzyme immobilization has been optimized at some conditions such as different GA values, different crosslinking times, different enzyme and pH values, and different times of immobilization. Results exhibited that the optimized immobilization conditions were obtained in 5.0% GA, after 4 h of crosslinking time, after 8 h immobilization time, using 210 mg protein/g support at pH 9.0. Based on these optimal conditions, the best encapsulation yield (EY) and activity recovery (AR) were obtained about 85% and 121.3%, respectively. The immobilized protease showed a 52% enhancement in protease activity than the free protease in pH 10. Furthermore, results displayed that the V max values of free and immobilized enzymes towards casein were gained 0.491 and 0.79 µmol/min, respectively. Moreover, the activity of immobilized protease was retained about 75% after incubation at 60 °C for 180 min at pH 9.0, in which the free protease only preserved about 20% of its primary activity. Results exhibited that the protease-NFs kept nearly 73% of its initial activity after three weeks of storage, while the free protease retained about 20% of its initial activity at the same condition. Results showed that the free protease exhibited 31% clot lysis, whereas the immobilized enzyme exhibited 39% clot lysis. The highest hydrolysis value of both proteases was done 17 and 48% after 4 h at 40 °C, respectively. These results indicated that Chit/CA electrospun nanofibres are excellent membranes for protease immobilization with high application in the digestion of protein waste.
{"title":"Protease immobilization on activated chitosan/cellulose acetate electrospun nanofibrous polymers: Biochemical characterization and efficient protein waste digestion","authors":"Arastoo Badoei-dalfard, Mahla Saeed, Z. Karami","doi":"10.1080/10242422.2022.2056450","DOIUrl":"https://doi.org/10.1080/10242422.2022.2056450","url":null,"abstract":"Abstract In this paper, a Serratia marcescens fibrinolytic protease KD was covalently immobilized onto the electrospun prepared glutaraldehyde (GA)-functionalized chitosan/cellulose acetate membrane nanofibres. Enzyme immobilization has been optimized at some conditions such as different GA values, different crosslinking times, different enzyme and pH values, and different times of immobilization. Results exhibited that the optimized immobilization conditions were obtained in 5.0% GA, after 4 h of crosslinking time, after 8 h immobilization time, using 210 mg protein/g support at pH 9.0. Based on these optimal conditions, the best encapsulation yield (EY) and activity recovery (AR) were obtained about 85% and 121.3%, respectively. The immobilized protease showed a 52% enhancement in protease activity than the free protease in pH 10. Furthermore, results displayed that the V max values of free and immobilized enzymes towards casein were gained 0.491 and 0.79 µmol/min, respectively. Moreover, the activity of immobilized protease was retained about 75% after incubation at 60 °C for 180 min at pH 9.0, in which the free protease only preserved about 20% of its primary activity. Results exhibited that the protease-NFs kept nearly 73% of its initial activity after three weeks of storage, while the free protease retained about 20% of its initial activity at the same condition. Results showed that the free protease exhibited 31% clot lysis, whereas the immobilized enzyme exhibited 39% clot lysis. The highest hydrolysis value of both proteases was done 17 and 48% after 4 h at 40 °C, respectively. These results indicated that Chit/CA electrospun nanofibres are excellent membranes for protease immobilization with high application in the digestion of protein waste.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"279 - 298"},"PeriodicalIF":1.8,"publicationDate":"2022-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49096601","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-03-30DOI: 10.1080/10242422.2022.2056451
Nidhi Singh, V. Singh, M. P. Singh
Abstract Biofuels are obtained from various renewable biological sources and considered suitable alternatives to conventional energy sources in the coming future. Biofuel is deemed essential to bioenergy, which can help achieve the 2030 agenda of United Nations Sustainable Development Goals (UNSDGs). Lignocellulosic materials convert into fermentable sugars by several pre-treatment methods. Several microbial lignocellulolytic enzymes play a significant role in degrading pre-treated lignocellulosic biomass into biofuels. These biomass-degrading enzymes have been screened only from a few cultured microorganisms. These problems related to biomass-degrading enzymes can be solved by screening novel microbial enzymes using metagenomic approaches.
{"title":"Microbial degradation of lignocellulosic biomass for bioenergy production: A metagenomic-based approach","authors":"Nidhi Singh, V. Singh, M. P. Singh","doi":"10.1080/10242422.2022.2056451","DOIUrl":"https://doi.org/10.1080/10242422.2022.2056451","url":null,"abstract":"Abstract Biofuels are obtained from various renewable biological sources and considered suitable alternatives to conventional energy sources in the coming future. Biofuel is deemed essential to bioenergy, which can help achieve the 2030 agenda of United Nations Sustainable Development Goals (UNSDGs). Lignocellulosic materials convert into fermentable sugars by several pre-treatment methods. Several microbial lignocellulolytic enzymes play a significant role in degrading pre-treated lignocellulosic biomass into biofuels. These biomass-degrading enzymes have been screened only from a few cultured microorganisms. These problems related to biomass-degrading enzymes can be solved by screening novel microbial enzymes using metagenomic approaches.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"15 - 25"},"PeriodicalIF":1.8,"publicationDate":"2022-03-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48962409","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-03-29DOI: 10.1080/10242422.2022.2055469
Rimple Chaudhary, Jyoti Kaushal, Gursharan Singh, A. Kaur, S. Arya
Abstract Along with the cellulase enzyme, xylanase plays an efficient role in the production of biofuel from agricultural wastes by degrading the xylan sugar present in the hemicellulose of cell wall. This study aims to improve the sugar production from biomass by the use of different enzymes with surfactant. The objective of this study is to compare sugar production and bioethanol production from sodium hydroxide along polyethylene glycol pre-treated paddy straw (Oryza sativa L.) with different combination of xylanase and cellulose enzymes along with lignin-degrading laccase enzyme. In results, 10.87 g/l of ethanol with saccharification of 64.51% ± 0.90 was obtained when xylanase and laccase were used, while 18.40 ± 0.56 g/l of ethanol with saccharification of 84.01%±1.09 was obtained when cellulase and laccase enzymes were used. Maximum bioethanol production was found to be 19.20 ± 0.26g/l, which was obtained by combination of xylanase, cellulase and laccase enzymes together at 37 °C after 36 h.
{"title":"Melioration of enzymatic ethanol production from alkali pre-treated paddy straw promoted by addition of surfactant","authors":"Rimple Chaudhary, Jyoti Kaushal, Gursharan Singh, A. Kaur, S. Arya","doi":"10.1080/10242422.2022.2055469","DOIUrl":"https://doi.org/10.1080/10242422.2022.2055469","url":null,"abstract":"Abstract Along with the cellulase enzyme, xylanase plays an efficient role in the production of biofuel from agricultural wastes by degrading the xylan sugar present in the hemicellulose of cell wall. This study aims to improve the sugar production from biomass by the use of different enzymes with surfactant. The objective of this study is to compare sugar production and bioethanol production from sodium hydroxide along polyethylene glycol pre-treated paddy straw (Oryza sativa L.) with different combination of xylanase and cellulose enzymes along with lignin-degrading laccase enzyme. In results, 10.87 g/l of ethanol with saccharification of 64.51% ± 0.90 was obtained when xylanase and laccase were used, while 18.40 ± 0.56 g/l of ethanol with saccharification of 84.01%±1.09 was obtained when cellulase and laccase enzymes were used. Maximum bioethanol production was found to be 19.20 ± 0.26g/l, which was obtained by combination of xylanase, cellulase and laccase enzymes together at 37 °C after 36 h.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"322 - 331"},"PeriodicalIF":1.8,"publicationDate":"2022-03-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41704703","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-03-15DOI: 10.1080/10242422.2022.2050707
C. Hámori, L. Kandra, G. Gyémánt
Abstract Potential of α-amylase from the gut of Leptinotarsa decemlineata (LDAmy) to catalyse transfer reactions was investigated. LDAmy as a component of insect gut extract showed significant transfer activity on reducing-end- and both-end-protected maltoheptamer substrates. Transfer reaction was examined using purified enzyme, 2-chloro-4-nitrophenyl β-d-glucopyranoside as acceptor and starch and maltooligosaccharides as donors. In addition to suitability of various donors, effect of pH and acetonitrile (MeCN) concentration were also studied. The reactions were followed using separation of reaction products by a reversed phase HPLC method. LDAmy catalysed the hydrolysis and transglycosylation of the both-end-protected substrate 4,6-O-benzylidene-4-nitrophenyl β-maltoheptaoside in parallel reactions. Shorter and longer both-end-protected products with degree of polymerization 4–10 were formed. Identification of products was carried out based on HPLC retention time, UV and mass spectra. Ratio of transglycosylation to hydrolysis reached 0.5 in presence of 20% MeCN as organic solvent. Aromatic protecting group at the non-reducing end was favourable for transfer reaction. Lack of the mobile loop and presence of more nonpolar aromatic moieties near to the active site may be the reason for the enhanced transfer activity of LDAmy based on the comparison of the sequence and structure of mammalian and insect-derived α-amylases. Highlights Transferase activity of Colorado potato beetle derived α-amylase LDAmy is presented. Effect of pH and organic co-solvent on transfer reaction of LDAmy were studied. Shorter and longer products were formed from a both-end protected maltoheptamer. The unusual transfer ability was explained by sequence differences of α-amylases.
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